Structural details of membrane-bound acetylcholine receptor from Tropedo marmorata.
- 1 February 1980
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 77 (2) , 952-956
- https://doi.org/10.1073/pnas.77.2.952
Abstract
A projection, at 15- to 20-.ANG. resolution, is presented of the structure of the membrane-bound acetylcholine receptor protein from T. marmorata. The projection has its axis perpendicular to the membrane plane; its main contribution originates from a hydrated portion of the protein, which extends from the membrane into the aqueous medium. The structure is distinctly asymmetric, with individual morphological subunits barely resolvable. These results were obtained by noncrystallographic averaging, using correlation functions, applied to electron micrographs of receptor-rich membrane fragments. The micrographs had been taken with minimal beam exposure in a scanning transmission electron microscopy.This publication has 16 references indexed in Scilit:
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